Fungal degradation of wood: initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate.
Identifieur interne : 000872 ( Main/Corpus ); précédent : 000871; suivant : 000873Fungal degradation of wood: initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate.
Auteurs : Ahmed Abbas ; Hasan Koc ; Feng Liu ; Ming TienSource :
- Current genetics [ 0172-8083 ] ; 2005.
English descriptors
- KwdEn :
- Cellulose (metabolism), Databases, Genetic (MeSH), Electrophoresis, Gel, Two-Dimensional (MeSH), Peptide Mapping (MeSH), Phanerochaete (genetics), Phanerochaete (physiology), Polysaccharides (metabolism), Proteomics (MeSH), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Wood (MeSH).
- MESH :
- chemical , metabolism : Cellulose, Polysaccharides.
- genetics : Phanerochaete.
- physiology : Phanerochaete.
- Databases, Genetic, Electrophoresis, Gel, Two-Dimensional, Peptide Mapping, Proteomics, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Wood.
Abstract
Two-dimensional (2-D) gel electrophoresis was used to separate the extracellular proteins produced by the white-rot fungus Phanerochaete chrysosporium. Solid-substrate cultures grown on red oak wood chips yielded extracellular protein preparations which were not suitable for 2-D gel analysis. However, pre-washing the wood chips with water helped decrease the amount of brown material which caused smearing on the acidic side of the isoelectric focusing gel. The 2-D gels from these wood-grown cultures revealed more than 45 protein spots. These spots were subjected to in-gel digestion with trypsin followed by either peptide fingerprint analysis by matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/MS) or by liquid chromatography (LC)/MS/MS sequencing. Data from both methods were analyzed by Protein Prospector and the local P. chrysosporium annotated database. MALDI-TOF/MS only identified two proteins out of 25 analyzed. This was most likely due to problems associated with glycosylation. Protein sequencing by LC/MS/MS of the same 25 proteins resulted in identification of 16 proteins. Most of the proteins identified act on either cellulose or hemicellulose or their hydrolysis products. Thus far no lignin peroxidase, Mn peroxidase or laccases have been detected.
DOI: 10.1007/s00294-004-0550-4
PubMed: 15551134
Links to Exploration step
pubmed:15551134Le document en format XML
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<author><name sortKey="Abbas, Ahmed" sort="Abbas, Ahmed" uniqKey="Abbas A" first="Ahmed" last="Abbas">Ahmed Abbas</name>
<affiliation><nlm:affiliation>Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.</nlm:affiliation>
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<author><name sortKey="Koc, Hasan" sort="Koc, Hasan" uniqKey="Koc H" first="Hasan" last="Koc">Hasan Koc</name>
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<author><name sortKey="Liu, Feng" sort="Liu, Feng" uniqKey="Liu F" first="Feng" last="Liu">Feng Liu</name>
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<author><name sortKey="Tien, Ming" sort="Tien, Ming" uniqKey="Tien M" first="Ming" last="Tien">Ming Tien</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Fungal degradation of wood: initial proteomic analysis of extracellular proteins of Phanerochaete chrysosporium grown on oak substrate.</title>
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<term>Peptide Mapping (MeSH)</term>
<term>Phanerochaete (genetics)</term>
<term>Phanerochaete (physiology)</term>
<term>Polysaccharides (metabolism)</term>
<term>Proteomics (MeSH)</term>
<term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Two-dimensional (2-D) gel electrophoresis was used to separate the extracellular proteins produced by the white-rot fungus Phanerochaete chrysosporium. Solid-substrate cultures grown on red oak wood chips yielded extracellular protein preparations which were not suitable for 2-D gel analysis. However, pre-washing the wood chips with water helped decrease the amount of brown material which caused smearing on the acidic side of the isoelectric focusing gel. The 2-D gels from these wood-grown cultures revealed more than 45 protein spots. These spots were subjected to in-gel digestion with trypsin followed by either peptide fingerprint analysis by matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/MS) or by liquid chromatography (LC)/MS/MS sequencing. Data from both methods were analyzed by Protein Prospector and the local P. chrysosporium annotated database. MALDI-TOF/MS only identified two proteins out of 25 analyzed. This was most likely due to problems associated with glycosylation. Protein sequencing by LC/MS/MS of the same 25 proteins resulted in identification of 16 proteins. Most of the proteins identified act on either cellulose or hemicellulose or their hydrolysis products. Thus far no lignin peroxidase, Mn peroxidase or laccases have been detected.</div>
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<Abstract><AbstractText>Two-dimensional (2-D) gel electrophoresis was used to separate the extracellular proteins produced by the white-rot fungus Phanerochaete chrysosporium. Solid-substrate cultures grown on red oak wood chips yielded extracellular protein preparations which were not suitable for 2-D gel analysis. However, pre-washing the wood chips with water helped decrease the amount of brown material which caused smearing on the acidic side of the isoelectric focusing gel. The 2-D gels from these wood-grown cultures revealed more than 45 protein spots. These spots were subjected to in-gel digestion with trypsin followed by either peptide fingerprint analysis by matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/MS) or by liquid chromatography (LC)/MS/MS sequencing. Data from both methods were analyzed by Protein Prospector and the local P. chrysosporium annotated database. MALDI-TOF/MS only identified two proteins out of 25 analyzed. This was most likely due to problems associated with glycosylation. Protein sequencing by LC/MS/MS of the same 25 proteins resulted in identification of 16 proteins. Most of the proteins identified act on either cellulose or hemicellulose or their hydrolysis products. Thus far no lignin peroxidase, Mn peroxidase or laccases have been detected.</AbstractText>
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